Summary:
Hydrogenase 1 mediates hydrogen uptake in the presence of high-potential acceptors such as ferricyanide and phenazine methosulfate, but not low-potential acceptors [Laurinavichene01]. The enzyme is more tolerant to oxygen than hydrogenase 2, providing complementary redox properties to the cell [Laurinavichene02, Lukey10, Wulff14].

Hydrogenase 1 contains a [3Fe-4S] or [4Fe-4S] cluster (depending on oxidation state) and nickel [DerVartanian96]. The substrate specificity of hydrogenase 1 for various quinones is unknown [Laurinavichene01].

HybG [Blokesch01] and HybF [Hube02] are involved in maturation of hydrogenase 1.

E. coli K-12 contains a second respiratory hydrogenase - hydrogenase 2 - and a third hydrogenase - hydrogenase 3 - which is part of the formate hydrogenlyase complex. A potential fourth hydrogenase - hydrogenase 4 - is encoded within the hyf operon. Only hydrogenase 1 can reduce nitroblue tetrazolium in anaerobically growing E. coli cells [Pinske12].

Enzymatic reaction of: hydrogenase

Summary:
There are four hydrogenases in E. coli which are synthesized in response to different physiological conditions. Hydrogenase 1 is a membrane-bound nickel-containing protein [Menon90, Sawers94]. It contains as electron-transfer components Fe-S clusters and nickel. It catalyzes the oxidation of hydrogen; the physiological electron carrier is unknown. The enzyme effects proton translocation coupled to the scalar redox reaction. [Sawers86]